ID B1I9S4_STRPI Unreviewed; 430 AA.
AC B1I9S4;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Maltose/maltodextrin transport system permease protein {ECO:0000256|RuleBase:RU367050};
GN OrderedLocusNames=SPH_2298 {ECO:0000313|EMBL:ACA36769.1};
OS Streptococcus pneumoniae (strain Hungary19A-6).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=487214 {ECO:0000313|EMBL:ACA36769.1, ECO:0000313|Proteomes:UP000002163};
RN [1] {ECO:0000313|Proteomes:UP000002163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungary19A-6 {ECO:0000313|Proteomes:UP000002163};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Probably responsible for the translocation
CC of the substrate across the membrane. {ECO:0000256|RuleBase:RU367050}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000256|ARBA:ARBA00009047,
CC ECO:0000256|RuleBase:RU367050}.
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DR EMBL; CP000936; ACA36769.1; -; Genomic_DNA.
DR RefSeq; WP_000414952.1; NC_010380.1.
DR AlphaFoldDB; B1I9S4; -.
DR KEGG; spv:SPH_2298; -.
DR HOGENOM; CLU_016047_0_3_9; -.
DR Proteomes; UP000002163; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-UniRule.
DR GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-UniRule.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR47314; MALTOSE/MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALF; 1.
DR PANTHER; PTHR47314:SF1; MALTOSE_MALTODEXTRIN TRANSPORT SYSTEM PERMEASE PROTEIN MALF; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF160964; MalF N-terminal region-like; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367050};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|RuleBase:RU367050};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 125..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 189..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 287..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 190..418
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 430 AA; 47733 MW; 6480DB8841355ECF CRC64;
MEKQQPSKAA LLSIIPGLGQ IYNKQKAKGF IFLGVTIVFV LYFLALAAPE LSNLITLGDK
PGRDNSLFML IRGAFHLIFV VVYVLFYFAN IKDAHTIAKR INNGIPVPRT LKDMIKGIYE
NGFPYLLIIP SYVAMTFAII FPVIVTLMIA FTNYDFQHLP PNKLLDWVGL TNFSNIWSLS
TFRSAFGSVL SWTIIWALAA STLQIVIGIF TAIIANQPFI KGKRIFGVIF LLPWAVPAFI
TILTFSNMFN DSVGAINTQV LPIFAKFLPF LDGALIPWKT DPTWTKIALI MMQGWLGFPY
IYVLTLGILQ SIPNDLYEAA YIDGANAWQK FRNITFPMIL AVAAPTLISQ YTFNFNNFSI
MYLFNGGGPG SVGGGAGSTD ILISWIYRLT TGTSPQYSMA AAVTLIISII VISISMIAFK
KLHAFDMEDV
//
